Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Proteins released during incubation in vitro of oviductal and uterine tissues from 8-week-old female NMRI mice treated neonatally with diethylstilbestrol (DES) or vehicle were studied. The objective was to study if neonatal DES treatment altered the patterns of proteins released from the oviduct and uterus, as earlier studies had shown a detrimental effect of the oviductal environment in DES exposed females on early embryo development. In separate experiments nonlabeled and 35S-labeled proteins released from oviductal/uterine tissues during organ incubations were characterized with 1 and 2D gel electrophoresis. The incubation media of both oviducts and uteri from DES females had increased levels of a serum derived nonlabeled protein, identified as apolipoprotein A1. The amount of this protein in the incubation medium was not influenced by previous ovariectomy but increased by in vivo treatment with estradiol, in both ovariectomized controls and DES treated females. Three other unlabeled proteins were consistently found in higher amounts in the incubation media from DES exposed oviduct/uterine tissue, than in incubates of control tissue. In tissue incubates of oviducts from DES females, three synthesized proteins (35 kDa-pl 6.2, 112 and 143 kDa) were released in lower amounts and two in higher amounts (53 kDa-pl 6.6 and 53 kDa-pl 6.8) than in controls. In uterus from DES treated females one labeled protein was released in increased amounts (80 kDa-pl 6.7) and one in decreased amounts (43 kDa-pl 6.6), when compared with controls. In estrogen induced uterine luminal fluid from 8-week-old DES treated females the levels of four proteins (26, 42, 53 and 97 kDa) were increased and two (24 and 32 kDa) were decreased. These results show permanent alterations in levels of secreted proteins in both the oviduct and uterus of adult but neonatally DES treated females, which could be of importance for their poor reproductive performance.
J Steroid Biochem Mol Biol 1993 Mar
PMID:Altered patterns of proteins released in vitro from oviductal and uterine tissue from adult female mice treated neonatally with diethylstilbestrol. 846 Dec 56

The catalytic subunit of protein phosphatase 2A (PP2Ac) was purified from Neurospora crassa extract by (NH4)2SO4-ethanol precipitation followed by DEAE-Sephacel, heparin-Sepharose, and MonoQ chromatography steps about 900-fold to a specific activity of 1200 U/g with a 2% yield. The apparent M(r) of PP2Ac was estimated to be 35 kDa by gel filtration and 33 kDa by SDS polyacrylamide gel electrophoresis. Half maximal inhibition of PP2Ac was achieved at 0.3 nM okadaic acid, 0.1 nM microcystin-LR, 56 nM cantharidin and 280 nM endothall concentrations. The preparation was completely inhibited by 20 mM NaF, was insensitive to rabbit muscle inhibitor-2, and was specific for the alpha-subunit of rabbit muscle phosphorylase kinase. According to its biochemical properties, N. crassa PP2Ac is very similar to its mammalian counterparts. Antipeptide antibodies raised against the N-terminal and C-terminal ends of human PP2Ac did not cross-react with N. crassa PP2Ac, indicating sequence differences outside the catalytic core of the enzyme.
Comp Biochem Physiol B Biochem Mol Biol 1995 Nov
PMID:Isolation and characterization of the catalytic subunit of protein phosphatase 2A from Neurospora crassa. 852 28

Neuronal cdc2-like kinase, nclk, is a heterodimer of cyclin dependent protein kinase 5, cdk5, and a 25 kDa subunit derived from a novel, neuron-specific, 35 kDa protein: p35. The characterization and regulation of nclk will be summarized in this minireview. The activity of nclk appears to be governed by highly complex regulatory mechanisms including protein-protein interaction, protein phosphorylation and isoforms. The histone H1 kinase activity of nclk is absolutely dependent of the interaction between the 25 kDa subunit and the catalytic subunit, cdk5. In addition, nclk interacts with other cellular proteins to form macromolecular complexes. The kinase activity of nclk is inhibited in vitro by the phosphorylation reactions of a weel-like protein tyrosine kinase and a protein serine/threonine kinase from bovine thymus. Northern blot analysis has revealed the existence of two populations of p35 mRNA of 2 and 4 kb. A novel cDNA encoding a p35 homologous protein has been obtained from a human hippocampus library.
Mol Cell Biochem
PMID:Regulatory properties of neuronal cdc2-like kinase. 856 47

S6 phosphatase activities, which dephosphorylate the phosphorylated S6 synthetic peptide, RRLSSLRASTSKSESSQK, were purified to near homogeneity from the membrane and cytosolic fractions of the rat parotid gland. Multiple S6 phosphatases were fractionated on Mono Q and gel filtration columns. In the cytosolic fraction, at least three forms of S6 phosphatase, termed peaks I, II, and III, were differentially resolved. The three forms had different sizes and protein compositions. The peak I enzyme, which had an approximately Mr of 68 kDa on gel filtration, appears to represent a dimeric form of the 39 kDa protein. This S6 phosphatase showed the high activity in the presence of EGTA and was completely inhibited by nanomolar concentrations of either okadaic acid or inhibitor 2. The peak II S6 phosphatase enzyme, with an Mr of 35 kDa, was activated by Mn2+. This form could be a proteolytic product of the catalytic subunit of type 1 phosphatase, due to its sensitivities to okadaic acid and inhibitor 2. The peak III enzyme, with an Mr of 55 kDa, is a Mn(2+)-dependent S6 phosphatase. This S6 phosphatase can be classified as a type 1 phosphatase, due to its sensitivity to okadaic acid, since the IC50 of okadaic acid is 4 nM. However, the molecular mass of this S6 phosphatase differs from that of the type 1 catalytic subunit (37 kDa) and showed less sensitivity to inhibitor 2. On the other hand, the membrane fraction contained one form of the S6 phosphatases, termed peak V (Mr 34 and 28 kDa), which could be classified as a type 1 phosphatase. This S6 phosphatase activity was greatly stimulated by Mn2+.
Mol Cell Biochem 1995 Jul 19
PMID:Purification and characterization of multiple S6 phosphatases from the rat parotid gland. 859 16

Human Alu-elements are short interspersed DNA sequences that comprise approximately 5% of the human genome. The physiological role of Alu-elements are unknown, although they are proposed to be involved in DNA replication, transcriptional regulation and nuclear transport of signal recognition particle RNA. Proteins that bind to Alu-element and Alu RNA have been identified in human cells. In HeLa cells, two proteins of 120 kDa and 35 kDa specifically bind to Alu-elements. We find that the 35 kDa protein is localized exclusively to the nucleus, while the 120 kDa protein is distributed between nucleus and cytoplasm. The 35 kDa protein is regulated by phosphorylation. Upon dephosphorylation, its DNA binding activity is significantly enhanced. Contrary to the recent identification of the smaller Alu-element binding protein as annexin II, we find that annexin II is not an Alu-element binding protein. Using a variety of techniques, we demonstrate that the 35 kDa Alu-element binding protein is distinct from annexin II.
Mol Cell Biochem 1996 Feb 23
PMID:Characterization of the HeLa cell 35 kDa Alu-element binding protein. 870 Jan 58

[3H]Choline mustard aziridinium ion binds irreversibly to the sodium-coupled high-affinity choline transport protein in a sodium-dependent and hemicholinium-sensitive manner, and thus is a useful affinity ligand. In rat striatal synaptosomal membranes, it radiolabels two polypeptides with apparent molecular masses of 58 and 35 kDa. Based upon the use of two different experimental approaches, it appears that neither of these polypeptides is glycosylated.
Brain Res Mol Brain Res 1996 Jan
PMID:Identification and partial characterization of the high-affinity choline carrier from rat brain striatum. 871 77

We have recently identified two different human DNA-binding proteins, SMBP1 (35 kDa) and SMBP2 (17 kDa), that specifically interact with the direct repeats of the enhancer sequence in the squirrel monkey retrovirus long terminal repeat. Herein, we report several biochemical properties of the human DNA-binding proteins. SMBP1 and 2 recognized an overlapped sequence of the 5' region of the repeat which contains a palindrome of CCAATGG. Both proteins required divalent cations such as Mg2+ and Ca2+ for their specific DNA binding at the optimum concentration of 1 mM. SMBP2 is a thermostable protein that binds tightly to the DNA sequence even by treatment at 80 degrees C for 15 min. The SMBP2-DNA complex was also stable in the presence of 300 mM NaCl. The resistance of SMBP2 to heat and salt treatment is a prominent character distinguishable from SMBP1 and other known transcriptional factors. SMBP1 and 2 can be easily separated by heparin-agarose chromatography. These DNA-binding proteins were found to be present in nuclear extracts from several human cell lines including T cell, B cell, and epithelial cell.
Cell Mol Biol (Noisy-le-grand) 1995 Dec
PMID:Characterization of human proteins that bind the repeated sequences in the squirrel monkey retrovirus enhancer. 874 92

Recently, there have been a number of reports showing a long-term increased expression of fos-related antigens (fra), molecular weight of 35 kDa, after brain injury or chronic treatment of rats with various drugs. We report elevated basal levels of this transcription factor in the olfactory bulb relative to other brain regions. The expression of this protein is further enhanced in the olfactory bulb as long as 3 months after a single injection of kainate, an effect similar to that we previously observed in the hippocampus. The AP-1 DNA binding activity in olfactory bulb from kainate-treated rats contains fra and jun immunoreactivity suggesting that the 35 kDa fra dimerizes with jun protein, probably junD, to bind to AP-1 sites. Elevated basal levels of this transcription factor in the olfactory bulb appear to be related to the constant reinnervation and synaptogenesis which occurs in this brain region. The 35 kDa fra may be involved in long-term genomic program changes required to adapt to an altered biochemical environment.
Brain Res Mol Brain Res 1995 Dec 01
PMID:Basal expression of 35 kDa fos-related antigen in olfactory bulb. 875 Aug 73

We have recently identified an antisense RNA (RNA alpha) that regulates the expression of the fatA iron transport gene encoding the outer membrane receptor for the iron-anguibactin complex. In this work, we demonstrate that RNA alpha also inhibits the expression of fatB, which encodes a 35 kDa iron transport protein and has domains homologous to other periplasmic transport proteins. The expression of fatA and fatB is repressed under iron-rich conditions, in which RNA alpha is induced. RNA alpha is homologous to two-thirds of the coding region of fatB. By cloning RNA alpha coding sequences immediately downstream of a tet promoter, we were able to obtain constitutive expression of the antisense RNA. The cloned region contains approximately 83% of the 650 nucleotide RNA alpha and is complementary to only 51% of the fatB mRNA but is still capable of causing a repression of the expression of the fatB gene. Our results in this work demonstrate that RNA alpha probably affects the stability of the fatB-specific mRNA.
Mol Microbiol 1995 Aug
PMID:Antisense RNA regulation of the fatB iron transport protein gene in Vibrio anguillarum. 880 28

The proteinase inhibitor set in skeletal muscle is poorly characterized at present. This study was aimed to investigate in mouse skeletal muscle 1) the tissue-associated counterpart, if any, of serum protease inhibitors (which may also play antiproteolytic functions in tissues) and 2) calpastatin, a tissue inhibitor of calcium-activated neutral proteases (calpains). Triton-extracts were prepared from muscle homogenates of mice, which had been perfused extensively with phosphate buffered saline (PBS) (under deep anesthesia) to remove blood inhibitors. Among various inhibitors tested, the following muscle-associated inhibitors were identified by western-blotting: alpha-2-macroglobulin (185, 165, 35 kDa), alpha-1-antitrypsin (52 kDa), inter-alpha-trypsin inhibitor (220, 180 kDa) and calpastatin (70 kDa). Combined light microscope and confocal immunohistochemical experiments revealed that, in all muscles examined (soleus, plantaris, extensor digitorum longus) the above specific immunoreactivities were localized outside the muscle fibers (in periendomysium, blood vessel wall) as well as within them. Inter-alpha-trypsin inhibitor, however, completely lacked the intracellular localization. This wide distribution of proteinase inhibitors suggests that numerous muscular structures may be normally protected from unwanted proteolysis, thus providing an essential background for further studies on pathological models with altered proteolysis (m. dystrophy, denervation atrophy, etc.).
Cell Mol Biol (Noisy-le-grand) 1996 Jun
PMID:Protease inhibitors in mouse skeletal muscle: tissue-associated components of serum inhibitors and calpastatin. 882 9


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